Enzymatic activities of Calloselasma rhodostoma (Malayan pit viper) venom

Tan, Nget-Hong; Kanthimathi, M.S.; Tan, Chon-Seng

doi:10.1016/0041-0101(86)90186-8

Cited by 25 publications

(12 citation statements)

References 14 publications

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“…L-amino acid oxidase activity was determined as described by Tan et al (33). Fifty microliters of horseradish peroxidase (100 purpurogalin unit/ mg) was added to 0.9 mL of 0.2 M triethanolamine buffer, pH 7.6, containing 0.1% L-leucine and 0.0075% o-dianidisine and incubated for three minutes at room temperature.…”

Section: L-amino Acid Oxidasementioning

confidence: 99%

“…Ion exchange chromatography separates proteins based on their ionic charges, and has been useful in snake venom fractionations as it does not affect the biological activity of eluted proteins, hence allowing their characterizations (33,38). With Resouce® Q column, an anion exchanger, H. hypnale venom was fractionated yielding twelve major fractions (Figure 1).…”

Section: Fractionation Of H Hypnale Venom Bymentioning

confidence: 99%

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Enzymatic and toxinological activities of Hypnale hypnale (hump-nosed pit viper) venom and its fractionation by ion exchange high performance liquid chromatography

Tan¹,

Sim²,

Gnanathasan³

et al. 2011

J. Venom. Anim. Toxins incl. Trop. Dis

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Abstract:Hypnale hypnale (hump-nosed pit viper) has been recently identified as one of the medically important venomous snakes in Sri Lanka and on the southwestern coast of India. The characterization of its venom is essential for understanding the pathophysiology of envenomation and for optimizing its management. In the present study, the biological properties of Hypnale hypnale venom and venom fractions obtained using Resource Q ion exchange chromatography were determined. The venom exhibited toxic activities typical of pit viper venom, comparable to that of its sister taxon, the Malayan pit viper (Calloselasma rhodostoma). Particularly noteworthy were its high activities of thrombin-like enzyme, proteases, phospholipase A 2 , L-amino acid oxidase and hyaluronidase. The thrombin-like enzyme was mainly acidic and distributed over several chromatography fractions, indicating its existence in multiple isoforms. The hemorrhagic and necrotic activities of the venom were likely associated with the proteolytic enzyme found mainly in the basic fraction. Phospholipase A 2 and phosphomonoesterase exist in both acidic and basic isoforms, while L-amino acid oxidase and hyaluronidase are highly acidic. The venom clotting activity on fibrinogens showed distinct species specificity in the following increasing order for clotting time: bovine < rabbit < goat < human < horse < < dog, and was comparable to that of C. rhodostoma venom. Its clot formation on human fibrinogen is gradual and prolonged, a phenomenon suggestive of consumptive coagulopathy as a complication observed clinically. At an intramuscular sublethal dose, the venom did not cause acute kidney injury in a rodent model, contrary to the positive control group treated with Daboia russelii venom. Nephrotoxicity may result from higher venom doses in the context of coagulopathy, as a complication provoked by venom hematoxicity.

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Section: L-amino Acid Oxidasementioning

confidence: 99%

Section: Fractionation Of H Hypnale Venom Bymentioning

confidence: 99%

Enzymatic and toxinological activities of Hypnale hypnale (hump-nosed pit viper) venom and its fractionation by ion exchange high performance liquid chromatography

Tan¹,

Sim²,

Gnanathasan³

et al. 2011

J. Venom. Anim. Toxins incl. Trop. Dis

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“…The venom causes local effects and systemic bleeding. Its venom has been reported to contain moderate to low levels of phospholipases A 2 (PLA 2 , E.C.3.1.1.4) [1]. However, the structure and activity of the venom PLA 2 s of this primitive monotypic pitviper were not known [2].…”

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confidence: 99%

Phospholipases A₂ from Callosellasma rhodostoma venom gland

Tsai

Wang

et al. 2000

European Journal of Biochemistry

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Callosellasma rhodostoma (Malayan pitviper) is a monotypic Asian pitviper of medical importance. Three acidic phospholipases A 2 (PLA 2 s) and one basic PLA 2 -homolog were purified from its venom while 10 cDNAs encoding distinct PLA 2 s were cloned from venom glands of a Thailand specimen of this species. Complete amino-acid sequences of the purified PLA 2 s were successfully deduced from their cDNA sequences. Among the six un-translated PLA 2 cDNAs, two apparently result from recombination of its Lys49-PLA 2 gene with its Asp49-PLA 2 genes. The acidic PLA 2 s inhibit platelet-aggregation, while the noncatalytic PLA 2 -homolog induces local edema. This basic PLA 2 -homolog contains both Asp49 and other, unusual substitutions unique for the venom Lys49-PLA 2 subtype (e.g. Leu5, Trp6, Asn28 and Arg34). Three-dimensional modelling of the basic protein revealed a heparin-binding region, and an abnormal calcium-binding pocket, which may explain its low catalytic activity. Oxidation of up to six of its Met residues or coinjection with heparin reduced its edemainducing activity but methylation of its active site His48 did not. The distinct Arg/Lys-rich and Met-rich region at positions 10±36 of the PLA 2 homolog presumably are involved in its heparin-binding and the cell membraneinterference leading to edema and myotoxicity.

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“…Proteolytic activity of CR and NK venoms was measured by modifying the methods of Kunitz (15) and Tan et al (16) One milliliter of 1% casein in 0.1 M Sorensen's phosphate buffer pH 7.6 and 1 mL of CR or NK venom (10-2500 µg) in the phosphate buffer were incubated for 30 min at 37 °C. The undigested casein was precipitated and the reaction terminated by adding 3 mL of 5% trichloroacetic acid.…”

Section: Proteasesmentioning

confidence: 99%

Anti-necrosis potential of polyphenols against snake venoms

Leanpolchareanchai

Pithayanukul

Bavovada

2009

Immunopharmacology and Immunotoxicology

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Polyphenols from the extracts of Areca catechu L. and Quercus infectoria Oliv. inhibited phospholipase A(2), proteases, hyaluronidase and L-amino acid oxidase of Naja naja kaouthia Lesson (NK) and Calloselasma rhodostoma Kuhl (CR) venoms by in vitro tests. Both extracts inhibited the hemorrhagic activity of CR venom and the dermonecrotic activity of NK venom by in vivo tests. The inhibitory activity of plant polyphenols against local tissue necrosis induced by snake venoms may be caused by inhibition of inflammatory reactions, hemorrhage, and necrosis. The result implies the therapeutic potential of plant polyphenols against necrosis in snakebite victims.

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Enzymatic activities of Calloselasma rhodostoma (Malayan pit viper) venom

Cited by 25 publications

References 14 publications

Enzymatic and toxinological activities of Hypnale hypnale (hump-nosed pit viper) venom and its fractionation by ion exchange high performance liquid chromatography

Enzymatic and toxinological activities of Hypnale hypnale (hump-nosed pit viper) venom and its fractionation by ion exchange high performance liquid chromatography

Phospholipases A₂ from Callosellasma rhodostoma venom gland

Anti-necrosis potential of polyphenols against snake venoms

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Enzymatic activities of Calloselasma rhodostoma (Malayan pit viper) venom

Cited by 25 publications

References 14 publications

Enzymatic and toxinological activities of Hypnale hypnale (hump-nosed pit viper) venom and its fractionation by ion exchange high performance liquid chromatography

Enzymatic and toxinological activities of Hypnale hypnale (hump-nosed pit viper) venom and its fractionation by ion exchange high performance liquid chromatography

Phospholipases A2 from Callosellasma rhodostoma venom gland

Anti-necrosis potential of polyphenols against snake venoms

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Phospholipases A₂ from Callosellasma rhodostoma venom gland